Nutrient chapter

Vanadium

Vanadium chemistry connects phosphate-sensitive enzymes, ion pumps, redox reactions and metal-binding proteins. Oxidation state, ligand, dose and experimental model determine the response; drug-like effects do not establish a dietary requirement.

62 recorded mechanisms · 4 availability situations · 7 preserved sources. Draft and verified records are labeled separately.

Read recorded mechanisms Open recursive mind map

The mechanisms

What the sources say this nutrient does, one relationship at a time. Plain wording comes first; the technical statement follows.

Vanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar.
Vanadate(V), protonation/speciation dependent → PTP1B preparation in the 1997 vanadate inhibition study source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract.
limitations
Assay affinity is not a dietary threshold, and PTP1B is not the only phosphatase inhibited.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery.
primary_references
Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 14–20
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract. · source_derived_draft · unverified_draft
## vanadium-ptp-competitive A phosphate-like inhibitor can occupy a phosphatase’s catalytic machinery. Vanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar. Model: Recombinant-enzyme kinetic study; construct species not resolved from accessed primary abstract. Limitations: Assay affinity is not a dietary threshold, and PTP1B is not the only phosphatase inhibited. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Complete structured claim and evidence
Adding EDTA immediately and completely reversed vanadate inhibition of PTP1B in the assay.
EDTA → PTP1B preparation in the 1997 vanadate inhibition study source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Enzyme assay with a vanadate-chelating reagent.
limitations
Biochemical reversal, not a clinical chelation treatment.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Removing available inhibitor restored activity in this preparation.
primary_references
Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 22–28
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Enzyme assay with a vanadate-chelating reagent. · source_derived_draft · unverified_draft
## vanadium-ptp-edta-reversal Removing available inhibitor restored activity in this preparation. Adding EDTA immediately and completely reversed vanadate inhibition of PTP1B in the assay. Model: Enzyme assay with a vanadate-chelating reagent. Limitations: Biochemical reversal, not a clinical chelation treatment. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Complete structured claim and evidence
Pervanadate irreversibly inhibited PTP1B by oxidation of its catalytic cysteine, supported by mass spectrometry.
Pervanadate / peroxovanadium(V) assay species → PTP1B preparation in the 1997 vanadate inhibition study source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Purified PTP1B kinetic and mass-spectrometric experiments.
limitations
Do not assign this irreversible oxidation to all vanadate exposures or dietary vanadium.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The peroxide-containing species disables the enzyme through a different mechanism.
primary_references
Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 30–36
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified PTP1B kinetic and mass-spectrometric experiments. · source_derived_draft · unverified_draft
## vanadium-pervanadate-cysteine The peroxide-containing species disables the enzyme through a different mechanism. Pervanadate irreversibly inhibited PTP1B by oxidation of its catalytic cysteine, supported by mass spectrometry. Model: Purified PTP1B kinetic and mass-spectrometric experiments. Limitations: Do not assign this irreversible oxidation to all vanadate exposures or dietary vanadium. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Complete structured claim and evidence
Dithiothreitol rapidly converted pervanadate to vanadate under the phosphatase assay conditions.
Dithiothreitol / DTT → Vanadate(V), protonation/speciation dependent source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cell-free reducing-agent experiment.
limitations
DTT is a laboratory reagent; glutathione cannot automatically be assigned identical kinetics.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The reducing environment can change which inhibitor is actually present.
primary_references
Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 38–44
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free reducing-agent experiment. · source_derived_draft · unverified_draft
## vanadium-dtt-speciation The reducing environment can change which inhibitor is actually present. Dithiothreitol rapidly converted pervanadate to vanadate under the phosphatase assay conditions. Model: Cell-free reducing-agent experiment. Limitations: DTT is a laboratory reagent; glutathione cannot automatically be assigned identical kinetics. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Complete structured claim and evidence
Catalase blocked the slow time-dependent inactivation seen under some vanadate conditions, supporting an in-situ peroxide/pervanadate contribution.
Catalase-treated PTP1B assay → Slow time-dependent PTP1B inactivation in vanadate assays source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
PTP1B time-course experiments with catalase.
limitations
Catalase rescue supports peroxide involvement; it does not identify every species in living cells.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
An assay can generate a second inhibitor while it runs.
primary_references
Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 46–52
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · PTP1B time-course experiments with catalase. · source_derived_draft · unverified_draft
## vanadium-catalase-artifact An assay can generate a second inhibitor while it runs. Catalase blocked the slow time-dependent inactivation seen under some vanadate conditions, supporting an in-situ peroxide/pervanadate contribution. Model: PTP1B time-course experiments with catalase. Limitations: Catalase rescue supports peroxide involvement; it does not identify every species in living cells. Evidence access: Primary abstract Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. · 1997 · https://pubmed.ncbi.nlm.nih.gov/8995372/ · DOI 10.1074/jbc.272.2.843
Complete structured claim and evidence
Vanadate and pervanadate stimulated glucose transport and GLUT movement to the plasma membrane in rat L6 myotubes.
Vanadate(V), protonation/speciation dependent → Glucose transport in vanadate-treated rat L6 myotubes source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat L6 myotubes; related rat H9c2 experiments used tagged GLUT4.
limitations
GLUT isoforms in the L6 result are not all resolved in the accessed abstract.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
More transporters at the surface can increase glucose entry.
primary_references
Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 54–60
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat L6 myotubes; related rat H9c2 experiments used tagged GLUT4. · source_derived_draft · unverified_draft
## vanadium-l6-transport More transporters at the surface can increase glucose entry. Vanadate and pervanadate stimulated glucose transport and GLUT movement to the plasma membrane in rat L6 myotubes. Model: Rat L6 myotubes; related rat H9c2 experiments used tagged GLUT4. Limitations: GLUT isoforms in the L6 result are not all resolved in the accessed abstract. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
Complete structured claim and evidence
Wortmannin inhibited measured PI3K signaling but did not block vanadate/pervanadate-stimulated glucose transport; it did block insulin-stimulated transport.
Wortmannin-sensitive PI3K inhibition in rat muscle cells → Glucose transport in vanadate-treated rat L6 myotubes source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat L6 and H9c2 cell inhibitor experiments.
limitations
Pharmacological context-specific result, not universal PI3K independence in every vanadium study.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The same transport outcome could be reached despite blocking a usual insulin pathway.
primary_references
Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 62–68
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat L6 and H9c2 cell inhibitor experiments. · source_derived_draft · unverified_draft
## vanadium-pi3k-not-required The same transport outcome could be reached despite blocking a usual insulin pathway. Wortmannin inhibited measured PI3K signaling but did not block vanadate/pervanadate-stimulated glucose transport; it did block insulin-stimulated transport. Model: Rat L6 and H9c2 cell inhibitor experiments. Limitations: Pharmacological context-specific result, not universal PI3K independence in every vanadium study. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
Complete structured claim and evidence
Vanadate at concentrations that maximally stimulated glucose transport did not significantly increase Akt activity, whereas pervanadate and insulin did.
Vanadate(V), protonation/speciation dependent → Rat Akt protein family, isoform unresolved source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat muscle-cell kinase assays.
limitations
Akt signal is not a surrogate for the complete glucose-transport response.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Chemical form changed signaling even when glucose transport increased.
primary_references
Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 70–76
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat muscle-cell kinase assays. · source_derived_draft · unverified_draft
## vanadium-akt-difference Chemical form changed signaling even when glucose transport increased. Vanadate at concentrations that maximally stimulated glucose transport did not significantly increase Akt activity, whereas pervanadate and insulin did. Model: Rat muscle-cell kinase assays. Limitations: Akt signal is not a surrogate for the complete glucose-transport response. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
Complete structured claim and evidence
Cytochalasin D-mediated actin disassembly blocked glucose-transport stimulation by vanadate, pervanadate and insulin.
Actin-network disruption in rat muscle cells → Glucose transport in vanadate-treated rat L6 myotubes source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_access
Primary abstract
experimental_model
Rat L6 myotube cytoskeleton perturbation.
limitations
Experimental machinery loss, not dietary deficiency.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The transport response still needed an intact cellular scaffold.
primary_references
Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
trigger_kind
machinery_impairment Imported condition classification; unverified.
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 78–84
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat L6 myotube cytoskeleton perturbation. · source_derived_draft · unverified_draft
## vanadium-actin-block The transport response still needed an intact cellular scaffold. Cytochalasin D-mediated actin disassembly blocked glucose-transport stimulation by vanadate, pervanadate and insulin. Model: Rat L6 myotube cytoskeleton perturbation. Limitations: Experimental machinery loss, not dietary deficiency. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
Complete structured claim and evidence
PKC inhibition or downregulation, alone or combined with wortmannin, failed to block vanadate/pervanadate-stimulated glucose transport.
PKC inhibition or downregulation in rat muscle cells → Glucose transport in vanadate-treated rat L6 myotubes source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat L6 inhibitor and prolonged-PMA experiments.
limitations
No conclusion about every PKC isoform in other cell types.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Blocking another signaling family did not remove the effect in these cells.
primary_references
Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 86–92
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat L6 inhibitor and prolonged-PMA experiments. · source_derived_draft · unverified_draft
## vanadium-pkc-block-null Blocking another signaling family did not remove the effect in these cells. PKC inhibition or downregulation, alone or combined with wortmannin, failed to block vanadate/pervanadate-stimulated glucose transport. Model: Rat L6 inhibitor and prolonged-PMA experiments. Limitations: No conclusion about every PKC isoform in other cell types. Evidence access: Primary abstract Tyrosine phosphatase inhibitors, vanadate and pervanadate, stimulate glucose transport and GLUT translocation in muscle cells by a mechanism independent of phosphatidylinositol 3-kinase and protein kinase C. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9792535/ · DOI 10.2337/diabetes.47.11.1676
Complete structured claim and evidence
Ascorbate generated V(IV) from vanadate in phosphate buffer at pH 7.4, but not comparably in water or the tested cacodylate buffer.
L-Ascorbate → Oxovanadium(IV) / vanadyl source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
ESR and spin-trapping chemistry; cell-free solutions.
limitations
Buffer-dependent chemistry does not establish a human depletion rate or clinical interaction.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Vitamin C and phosphate together changed vanadium’s oxidation state in this assay.
primary_references
One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 94–100
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · ESR and spin-trapping chemistry; cell-free solutions. · source_derived_draft · unverified_draft
## vanadium-ascorbate-reduction Vitamin C and phosphate together changed vanadium’s oxidation state in this assay. Ascorbate generated V(IV) from vanadate in phosphate buffer at pH 7.4, but not comparably in water or the tested cacodylate buffer. Model: ESR and spin-trapping chemistry; cell-free solutions. Limitations: Buffer-dependent chemistry does not establish a human depletion rate or clinical interaction. Evidence access: Primary abstract One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1
Complete structured claim and evidence
In phosphate/ascorbate mixtures with peroxide, reduced vanadium supported hydroxyl-radical generation; omitting phosphate sharply reduced the yield.
Oxovanadium(IV) / vanadyl → Hydroxyl-radical generation in vanadium redox assays source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cell-free ESR spin trapping.
limitations
Chemical mechanism under specified reagents; not proof that vitamin C supplementation causes this injury in people.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A reductant can enable pro-oxidant chemistry when peroxide is also present.
primary_references
One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 102–108
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free ESR spin trapping. · source_derived_draft · unverified_draft
## vanadium-peroxide-radicals A reductant can enable pro-oxidant chemistry when peroxide is also present. In phosphate/ascorbate mixtures with peroxide, reduced vanadium supported hydroxyl-radical generation; omitting phosphate sharply reduced the yield. Model: Cell-free ESR spin trapping. Limitations: Chemical mechanism under specified reagents; not proof that vitamin C supplementation causes this injury in people. Evidence access: Primary abstract One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1
Complete structured claim and evidence
V(IV) generated by ascorbate/vanadate chemistry produced hydroperoxide-derived radicals from cumene hydroperoxide.
Oxovanadium(IV) / vanadyl → Radicals derived from hydroperoxide in vanadium assays source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cell-free model-hydroperoxide assay.
limitations
Cumene hydroperoxide is a model reagent, not direct measurement of membrane injury in humans.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The same redox system can also react with a model lipid peroxide.
primary_references
One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 110–116
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free model-hydroperoxide assay. · source_derived_draft · unverified_draft
## vanadium-lipid-peroxide-radicals The same redox system can also react with a model lipid peroxide. V(IV) generated by ascorbate/vanadate chemistry produced hydroperoxide-derived radicals from cumene hydroperoxide. Model: Cell-free model-hydroperoxide assay. Limitations: Cumene hydroperoxide is a model reagent, not direct measurement of membrane injury in humans. Evidence access: Primary abstract One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. · 1994 · https://pubmed.ncbi.nlm.nih.gov/8051539/ · DOI 10.1016/0162-0134(94)85032-1
Complete structured claim and evidence
A vanadate/ascorbate/phosphate system oxidized NADH, with similar results for NADPH, through a proposed superoxide-initiated chain reaction.
Vanadate(V), protonation/speciation dependent → NADH source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cell-free NADH/NADPH oxidation experiments.
limitations
Not evidence of a measured whole-body NAD shortage.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Reducing equivalents can be consumed by a metal-dependent reaction.
primary_references
Vanadate-mediated oxidation of NADH: description of an in vitro system requiring ascorbate and phosphate. · 1989 · https://pubmed.ncbi.nlm.nih.gov/2735768/ · DOI 10.1016/0003-9861(89)90196-3
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 118–124
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free NADH/NADPH oxidation experiments. · source_derived_draft · unverified_draft
## vanadium-nadh-oxidation Reducing equivalents can be consumed by a metal-dependent reaction. A vanadate/ascorbate/phosphate system oxidized NADH, with similar results for NADPH, through a proposed superoxide-initiated chain reaction. Model: Cell-free NADH/NADPH oxidation experiments. Limitations: Not evidence of a measured whole-body NAD shortage. Evidence access: Primary abstract Vanadate-mediated oxidation of NADH: description of an in vitro system requiring ascorbate and phosphate. · 1989 · https://pubmed.ncbi.nlm.nih.gov/2735768/ · DOI 10.1016/0003-9861(89)90196-3
Complete structured claim and evidence
Superoxide dismutase inhibited NADH oxidation in the vanadate/ascorbate/phosphate system, whereas catalase and ethanol did not.
Superoxide-dismutase-treated vanadium redox assay → NADH oxidation in the vanadium chemical assay source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cell-free scavenger comparison.
limitations
Does not imply catalase is irrelevant to all vanadium toxicity.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The scavenger comparison points to a superoxide-dependent step in this particular reaction.
primary_references
Vanadate-mediated oxidation of NADH: description of an in vitro system requiring ascorbate and phosphate. · 1989 · https://pubmed.ncbi.nlm.nih.gov/2735768/ · DOI 10.1016/0003-9861(89)90196-3
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 126–132
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free scavenger comparison. · source_derived_draft · unverified_draft
## vanadium-sod-redox-rescue The scavenger comparison points to a superoxide-dependent step in this particular reaction. Superoxide dismutase inhibited NADH oxidation in the vanadate/ascorbate/phosphate system, whereas catalase and ethanol did not. Model: Cell-free scavenger comparison. Limitations: Does not imply catalase is irrelevant to all vanadium toxicity. Evidence access: Primary abstract Vanadate-mediated oxidation of NADH: description of an in vitro system requiring ascorbate and phosphate. · 1989 · https://pubmed.ncbi.nlm.nih.gov/2735768/ · DOI 10.1016/0003-9861(89)90196-3
Complete structured claim and evidence
Ascorbate initiated NADH oxidation at lower concentrations but inhibited it at higher concentrations in the same chemical system.
L-Ascorbate → NADH oxidation in the vanadium chemical assay source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cell-free concentration-response experiments.
limitations
Not an established supplement dose-response in humans.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The direction of an antioxidant’s effect can depend on concentration.
primary_references
Vanadate-mediated oxidation of NADH: description of an in vitro system requiring ascorbate and phosphate. · 1989 · https://pubmed.ncbi.nlm.nih.gov/2735768/ · DOI 10.1016/0003-9861(89)90196-3
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 134–140
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free concentration-response experiments. · source_derived_draft · unverified_draft
## vanadium-ascorbate-concentration The direction of an antioxidant’s effect can depend on concentration. Ascorbate initiated NADH oxidation at lower concentrations but inhibited it at higher concentrations in the same chemical system. Model: Cell-free concentration-response experiments. Limitations: Not an established supplement dose-response in humans. Evidence access: Primary abstract Vanadate-mediated oxidation of NADH: description of an in vitro system requiring ascorbate and phosphate. · 1989 · https://pubmed.ncbi.nlm.nih.gov/2735768/ · DOI 10.1016/0003-9861(89)90196-3
Complete structured claim and evidence
Glutathione and catalase reversed vanadate sensitivity in the susceptible cell line studied.
GSH → Viability in the vanadate-sensitive cell-line experiment source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Two cell lines with different susceptibilities; identities not provided in accessed abstract.
limitations
The proposed intracellular peroxovanadium sequence was not established as a universal mechanism.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Available reducing or peroxide-removing capacity changed the toxicity response.
primary_references
Mechanisms of vanadate-induced cellular toxicity: role of cellular glutathione and NADPH. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12234491/ · DOI 10.1016/s0003-9861(02)00408-3
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 142–148
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Two cell lines with different susceptibilities; identities not provided in accessed abstract. · source_derived_draft · unverified_draft
## vanadium-gsh-cell-rescue Available reducing or peroxide-removing capacity changed the toxicity response. Glutathione and catalase reversed vanadate sensitivity in the susceptible cell line studied. Model: Two cell lines with different susceptibilities; identities not provided in accessed abstract. Limitations: The proposed intracellular peroxovanadium sequence was not established as a universal mechanism. Evidence access: Primary abstract Mechanisms of vanadate-induced cellular toxicity: role of cellular glutathione and NADPH. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12234491/ · DOI 10.1016/s0003-9861(02)00408-3
Complete structured claim and evidence
NADPH sensitized vanadate-resistant cells and increased phosphotyrosine signals and Ras expression in the reported experiment.
NADPH → Vanadate sensitization of a resistant cell line source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Cell-line NADPH intervention.
limitations
Changes support redox-dependent signaling but do not directly demonstrate each proposed vanadium intermediate.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
More reducing power did not necessarily protect against this metal exposure.
primary_references
Mechanisms of vanadate-induced cellular toxicity: role of cellular glutathione and NADPH. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12234491/ · DOI 10.1016/s0003-9861(02)00408-3
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 150–156
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-line NADPH intervention. · source_derived_draft · unverified_draft
## vanadium-nadph-sensitization More reducing power did not necessarily protect against this metal exposure. NADPH sensitized vanadate-resistant cells and increased phosphotyrosine signals and Ras expression in the reported experiment. Model: Cell-line NADPH intervention. Limitations: Changes support redox-dependent signaling but do not directly demonstrate each proposed vanadium intermediate. Evidence access: Primary abstract Mechanisms of vanadate-induced cellular toxicity: role of cellular glutathione and NADPH. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12234491/ · DOI 10.1016/s0003-9861(02)00408-3
Complete structured claim and evidence
Vanadate exposure depleted intracellular nonprotein sulfhydryls while increasing extracellular glutathione in human erythrocytes.
Vanadate(V), protonation/speciation dependent → Glutathione efflux from vanadate-exposed human erythrocytes source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Isolated human erythrocytes; millimolar vanadate exposures up to four hours.
limitations
High ex-vivo concentrations; nonprotein sulfhydryl assays are not exclusively glutathione measurements.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Loss of an intracellular thiol pool can include export rather than only oxidation.
primary_references
Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 158–164
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Isolated human erythrocytes; millimolar vanadate exposures up to four hours. · source_derived_draft · unverified_draft
## vanadium-erythrocyte-gsh Loss of an intracellular thiol pool can include export rather than only oxidation. Vanadate exposure depleted intracellular nonprotein sulfhydryls while increasing extracellular glutathione in human erythrocytes. Model: Isolated human erythrocytes; millimolar vanadate exposures up to four hours. Limitations: High ex-vivo concentrations; nonprotein sulfhydryl assays are not exclusively glutathione measurements. Evidence access: Primary abstract Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
Complete structured claim and evidence
DIDS inhibited the intracellular thiol decrease and extracellular increase during vanadate exposure, supporting an anion-transport-dependent step.
Human erythrocyte anion exchanger 1 / SLC4A1 → Glutathione efflux from vanadate-exposed human erythrocytes source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_access
Primary abstract
experimental_model
Human erythrocytes; DIDS pharmacological intervention.
limitations
DIDS is an inhibitor, not itself an exchanger; pharmacology does not establish a unique SLC4A1 transport substrate or route.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Membrane transport can gate the redox response.
primary_references
Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
trigger_kind
machinery_impairment Imported condition classification; unverified.
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 166–172
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human erythrocytes; DIDS pharmacological intervention. · source_derived_draft · unverified_draft
## vanadium-anion-exchanger-block Membrane transport can gate the redox response. DIDS inhibited the intracellular thiol decrease and extracellular increase during vanadate exposure, supporting an anion-transport-dependent step. Model: Human erythrocytes; DIDS pharmacological intervention. Limitations: DIDS is an inhibitor, not itself an exchanger; pharmacology does not establish a unique SLC4A1 transport substrate or route. Evidence access: Primary abstract Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
Complete structured claim and evidence
MK571 reduced glutathione efflux during erythrocyte vanadate exposure, suggesting involvement of an MRP-family exporter.
MRP-inhibitor experiment in human erythrocytes → Glutathione efflux from vanadate-exposed human erythrocytes source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_access
Primary abstract
experimental_model
Human erythrocyte inhibitor experiment.
limitations
The accessed study does not identify a specific ABCC isoform; no invented transporter assignment.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
An exporter can contribute to loss of cellular glutathione.
primary_references
Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
trigger_kind
machinery_impairment Imported condition classification; unverified.
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 174–180
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human erythrocyte inhibitor experiment. · source_derived_draft · unverified_draft
## vanadium-mrp-efflux-block An exporter can contribute to loss of cellular glutathione. MK571 reduced glutathione efflux during erythrocyte vanadate exposure, suggesting involvement of an MRP-family exporter. Model: Human erythrocyte inhibitor experiment. Limitations: The accessed study does not identify a specific ABCC isoform; no invented transporter assignment. Evidence access: Primary abstract Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
Complete structured claim and evidence
DMSA treatment of erythrocyte supernatants increased measured glutathione, consistent with release from metal-associated forms.
Dimercaptosuccinic acid / DMSA → Recoverable extracellular glutathione after vanadate exposure source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Ex-vivo supernatant treatment.
limitations
This supports but does not structurally identify every GSH–vanadium complex; not clinical chelation guidance.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
An assay can detect additional glutathione after a complex is disrupted.
primary_references
Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 182–188
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Ex-vivo supernatant treatment. · source_derived_draft · unverified_draft
## vanadium-gsh-complex-recovery An assay can detect additional glutathione after a complex is disrupted. DMSA treatment of erythrocyte supernatants increased measured glutathione, consistent with release from metal-associated forms. Model: Ex-vivo supernatant treatment. Limitations: This supports but does not structurally identify every GSH–vanadium complex; not clinical chelation guidance. Evidence access: Primary abstract Efflux of glutathione and glutathione complexes from human erythrocytes in response to vanadate. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22824382/ · DOI 10.1016/j.bcmd.2012.07.001
Complete structured claim and evidence
V(V) and V(IV) bound vacant transferrin iron-binding sites in culture medium even with a 20-fold molar excess of albumin, without displacing already-bound Fe(III) under those conditions.
Vanadate(V), protonation/speciation dependent → Human serum transferrin / TF source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human transferrin binding experiments under normoxic conditions.
limitations
Does not establish systemic iron deficiency or competition magnitude at dietary exposures.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Vanadium can occupy available metal-binding sites without stripping out all bound iron.
primary_references
Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 190–196
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transferrin binding experiments under normoxic conditions. · source_derived_draft · unverified_draft
## vanadium-tf-binding Vanadium can occupy available metal-binding sites without stripping out all bound iron. V(V) and V(IV) bound vacant transferrin iron-binding sites in culture medium even with a 20-fold molar excess of albumin, without displacing already-bound Fe(III) under those conditions. Model: Human transferrin binding experiments under normoxic conditions. Limitations: Does not establish systemic iron deficiency or competition magnitude at dietary exposures. Evidence access: Primary abstract Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926
Complete structured claim and evidence
Transferrin binding reduced vanadium uptake and antiproliferative activity in human A549 cells.
Human transferrin bound to vanadium(V/IV) → Vanadium uptake in human A549 cells source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human lung-cancer cell uptake and proliferation assays.
limitations
Does not establish every tissue’s uptake route or clinical efficacy.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Binding to a carrier protein can reduce delivery rather than improve it.
primary_references
Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 198–204
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human lung-cancer cell uptake and proliferation assays. · source_derived_draft · unverified_draft
## vanadium-tf-uptake-reduction Binding to a carrier protein can reduce delivery rather than improve it. Transferrin binding reduced vanadium uptake and antiproliferative activity in human A549 cells. Model: Human lung-cancer cell uptake and proliferation assays. Limitations: Does not establish every tissue’s uptake route or clinical efficacy. Evidence access: Primary abstract Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926
Complete structured claim and evidence
Vanadium binding did not increase transferrin affinity for TfR1 at pH 7.4, but disrupted conformational changes at pH 5.6 with citrate in the transferrin-cycle model.
Human transferrin bound to vanadium(V/IV) → Endosome-like conformational change of vanadium-bound human transferrin source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Biolayer interferometry and electrophoretic model of the human transferrin cycle.
limitations
Return of undissociated V–transferrin to the surface is the authors’ proposed explanation, not directly imaged trafficking.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Receptor recognition and release during endosomal processing are different steps.
primary_references
Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 206–212
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Biolayer interferometry and electrophoretic model of the human transferrin cycle. · source_derived_draft · unverified_draft
## vanadium-tf-cycle Receptor recognition and release during endosomal processing are different steps. Vanadium binding did not increase transferrin affinity for TfR1 at pH 7.4, but disrupted conformational changes at pH 5.6 with citrate in the transferrin-cycle model. Model: Biolayer interferometry and electrophoretic model of the human transferrin cycle. Limitations: Return of undissociated V–transferrin to the surface is the authors’ proposed explanation, not directly imaged trafficking. Evidence access: Primary abstract Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926
Complete structured claim and evidence
Crystals of C-lobe-ferric human transferrin exposed to vanadyl acetylacetonate contained a two-vanadium(V) unit linked to Tyr188 rather than intact V(IV) acetylacetonate.
Bis(acetylacetonato)oxovanadium(IV) → Human C-lobe-ferric transferrin Tyr188-linked divanadate(V) adduct source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text
experimental_model
Human protein crystallography; 5 mM compound and crystallization conditions.
limitations
Reaction/crystal structure does not demonstrate the same species dominates human blood.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The species bound to a protein can differ from the compound originally added.
primary_references
First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 214–220
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human protein crystallography; 5 mM compound and crystallization conditions. · source_derived_draft · unverified_draft
## vanadium-tf-crystal-transformation The species bound to a protein can differ from the compound originally added. Crystals of C-lobe-ferric human transferrin exposed to vanadyl acetylacetonate contained a two-vanadium(V) unit linked to Tyr188 rather than intact V(IV) acetylacetonate. Model: Human protein crystallography; 5 mM compound and crystallization conditions. Limitations: Reaction/crystal structure does not demonstrate the same species dominates human blood. Evidence access: Primary full text First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1
Complete structured claim and evidence
The vanadium adduct retained an open N-lobe and closed iron-containing C-lobe with little overall structural change.
Human C-lobe-ferric transferrin Tyr188-linked divanadate(V) adduct → Open N-lobe conformation of monoferric human transferrin source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text
experimental_model
Human transferrin crystal comparison.
limitations
Compatibility with receptor recognition is a structural interpretation, not a completed cellular uptake cycle; not a contradiction of the A549 transport study.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A binding structure alone does not demonstrate successful cellular delivery.
primary_references
First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 222–228
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transferrin crystal comparison. · source_derived_draft · unverified_draft
## vanadium-tf-open-lobe A binding structure alone does not demonstrate successful cellular delivery. The vanadium adduct retained an open N-lobe and closed iron-containing C-lobe with little overall structural change. Model: Human transferrin crystal comparison. Limitations: Compatibility with receptor recognition is a structural interpretation, not a completed cellular uptake cycle; not a contradiction of the A549 transport study. Evidence access: Primary full text First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1
Complete structured claim and evidence
Replacing 3 mM MgCl2 with MnCl2 lowered vanadate-binding Kd from 96 to 12 nM in the dog-kidney Na/K-ATPase preparation without changing binding capacity.
Mn2+ → Dog kidney sodium/potassium ATPase preparation source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Dog kidney particulate-enzyme radiovanadate binding assay.
limitations
Assay concentrations and enzyme state matter; not a manganese supplementation interaction in humans.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The supporting divalent ion changed inhibitor affinity.
primary_references
Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 230–236
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Dog kidney particulate-enzyme radiovanadate binding assay. · source_derived_draft · unverified_draft
## vanadium-pump-mg-mn The supporting divalent ion changed inhibitor affinity. Replacing 3 mM MgCl2 with MnCl2 lowered vanadate-binding Kd from 96 to 12 nM in the dog-kidney Na/K-ATPase preparation without changing binding capacity. Model: Dog kidney particulate-enzyme radiovanadate binding assay. Limitations: Assay concentrations and enzyme state matter; not a manganese supplementation interaction in humans. Evidence access: Primary abstract Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200
Complete structured claim and evidence
In magnesium-containing medium, potassium increased vanadate binding and lowered its Kd to about 11 nM without changing maximum binding.
Potassium ion → Dog kidney sodium/potassium ATPase preparation source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Dog kidney Na/K-ATPase binding experiments.
limitations
Effect was not appreciable under the manganese condition; not evidence that dietary potassium necessarily increases toxicity.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Potassium can shift the pump toward an inhibitor-sensitive state.
primary_references
Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 238–244
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Dog kidney Na/K-ATPase binding experiments. · source_derived_draft · unverified_draft
## vanadium-pump-potassium Potassium can shift the pump toward an inhibitor-sensitive state. In magnesium-containing medium, potassium increased vanadate binding and lowered its Kd to about 11 nM without changing maximum binding. Model: Dog kidney Na/K-ATPase binding experiments. Limitations: Effect was not appreciable under the manganese condition; not evidence that dietary potassium necessarily increases toxicity. Evidence access: Primary abstract Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200
Complete structured claim and evidence
Sodium decreased vanadate binding in magnesium-containing medium, whereas sodium and potassium had little effect in the manganese condition.
Sodium ion → Dog kidney sodium/potassium ATPase preparation source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Dog kidney enzyme binding assay.
limitations
No human dietary sodium recommendation follows.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The ionic environment changes how vanadate interacts with the pump.
primary_references
Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 246–252
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Dog kidney enzyme binding assay. · source_derived_draft · unverified_draft
## vanadium-pump-sodium The ionic environment changes how vanadate interacts with the pump. Sodium decreased vanadate binding in magnesium-containing medium, whereas sodium and potassium had little effect in the manganese condition. Model: Dog kidney enzyme binding assay. Limitations: No human dietary sodium recommendation follows. Evidence access: Primary abstract Vanadate binding to the (Na + K)-ATPase. · 1981 · https://pubmed.ncbi.nlm.nih.gov/6277881/ · DOI 10.1007/BF00743200
Complete structured claim and evidence
Vanadate occupied the catalytic site of calcium-free SERCA as planar VO3 with water and magnesium in a dephosphorylation-transition-like conformation.
Vanadate(V), protonation/speciation dependent → Rabbit SERCA1a / ATP2A1 source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract and RCSB PDB 5A3Q author deposition
experimental_model
Rabbit SERCA structure, deposition 5A3Q; primary abstract plus author-deposited structure identity.
limitations
Structure used nucleotide analogues and thapsigargin; not a measured human intracellular calcium effect.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A phosphate analogue can trap a calcium pump in a catalytic state.
primary_references
Crystal Structure of the Vanadate-Inhibited Ca(2+)-ATPase. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27050689/ · DOI 10.1016/j.str.2016.02.018
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 254–260
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rabbit SERCA structure, deposition 5A3Q; primary abstract plus author-deposited structure identity. · source_derived_draft · unverified_draft
## vanadium-serca-transition A phosphate analogue can trap a calcium pump in a catalytic state. Vanadate occupied the catalytic site of calcium-free SERCA as planar VO3 with water and magnesium in a dephosphorylation-transition-like conformation. Model: Rabbit SERCA structure, deposition 5A3Q; primary abstract plus author-deposited structure identity. Limitations: Structure used nucleotide analogues and thapsigargin; not a measured human intracellular calcium effect. Evidence access: Primary abstract and RCSB PDB 5A3Q author deposition Crystal Structure of the Vanadate-Inhibited Ca(2+)-ATPase. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27050689/ · DOI 10.1016/j.str.2016.02.018
Complete structured claim and evidence
Vanadate crystallization of rat-liver F1 ATP synthase captured an ADP–vanadate–Mg transition-like state with remodeling of the catalytic P-loop region.
Vanadate(V), protonation/speciation dependent → Rat liver F1 ATP synthase catalytic unit source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat liver F1 crystallography.
limitations
A captured structure is not proof that a given oral dose suppresses mitochondrial ATP production.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Another ATP-handling enzyme can bind the phosphate analogue.
primary_references
Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16531409/ · DOI 10.1074/jbc.M513369200
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 262–268
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat liver F1 crystallography. · source_derived_draft · unverified_draft
## vanadium-f1-transition Another ATP-handling enzyme can bind the phosphate analogue. Vanadate crystallization of rat-liver F1 ATP synthase captured an ADP–vanadate–Mg transition-like state with remodeling of the catalytic P-loop region. Model: Rat liver F1 crystallography. Limitations: A captured structure is not proof that a given oral dose suppresses mitochondrial ATP production. Evidence access: Primary abstract Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16531409/ · DOI 10.1074/jbc.M513369200
Complete structured claim and evidence
In the vanadate-inhibited human ARSB structure, vanadate replaced sulfate at the active site and was covalently linked to the modified catalytic residue.
Vanadate(V), protonation/speciation dependent → Human N-acetylgalactosamine-4-sulfatase / ARSB source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human lysosomal sulfatase crystallography.
limitations
Structural inhibition is not evidence that oral vanadium causes mucopolysaccharidosis.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Vanadium’s targets extend beyond insulin signaling and ATPases.
primary_references
Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 270–276
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human lysosomal sulfatase crystallography. · source_derived_draft · unverified_draft
## vanadium-sulfatase-binding Vanadium’s targets extend beyond insulin signaling and ATPases. In the vanadate-inhibited human ARSB structure, vanadate replaced sulfate at the active site and was covalently linked to the modified catalytic residue. Model: Human lysosomal sulfatase crystallography. Limitations: Structural inhibition is not evidence that oral vanadium causes mucopolysaccharidosis. Evidence access: Primary abstract Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
Complete structured claim and evidence
Human ARSB crystallography identified calcium coordinated in the sulfate-containing catalytic site and an essential modified Cys91 residue.
Calcium ion → Human N-acetylgalactosamine-4-sulfatase / ARSB source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human lysosomal sulfatase structure.
limitations
Does not show calcium supplementation reverses vanadate inhibition.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Calcium and enzyme maturation define the machinery that the inhibitor encounters.
primary_references
Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 278–284
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human lysosomal sulfatase structure. · source_derived_draft · unverified_draft
## vanadium-sulfatase-calcium Calcium and enzyme maturation define the machinery that the inhibitor encounters. Human ARSB crystallography identified calcium coordinated in the sulfate-containing catalytic site and an essential modified Cys91 residue. Model: Human lysosomal sulfatase structure. Limitations: Does not show calcium supplementation reverses vanadate inhibition. Evidence access: Primary abstract Structure of a human lysosomal sulfatase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9032078/ · DOI 10.1016/s0969-2126(97)00185-8
Complete structured claim and evidence
Decavanadate and mixed metavanadate solutions depolarized mitochondria in neonatal rat cardiomyocytes within six hours; half-maximal depolarization occurred near 6.5 micromolar total vanadium.
Decavanadate(V) → Mitochondrial depolarization in vanadate-exposed neonatal rat cardiomyocytes source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Neonatal rat cardiomyocytes; fluorescent membrane-potential probes.
limitations
Total vanadium differs from decamer concentration: 6.5 micromolar total V equals 0.65 micromolar V10. No human threshold is established.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Mitochondrial electrical failure preceded later cell death.
primary_references
Vanadate induces necrotic death in neonatal rat cardiomyocytes through mitochondrial membrane depolarization. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18251508/ · DOI 10.1021/tx700204r
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Neonatal rat cardiomyocytes; fluorescent membrane-potential probes. · source_derived_draft · unverified_draft
## vanadium-cardiac-depolarization Mitochondrial electrical failure preceded later cell death. Decavanadate and mixed metavanadate solutions depolarized mitochondria in neonatal rat cardiomyocytes within six hours; half-maximal depolarization occurred near 6.5 micromolar total vanadium. Model: Neonatal rat cardiomyocytes; fluorescent membrane-potential probes. Limitations: Total vanadium differs from decamer concentration: 6.5 micromolar total V equals 0.65 micromolar V10. No human threshold is established. Evidence access: Primary abstract Vanadate induces necrotic death in neonatal rat cardiomyocytes through mitochondrial membrane depolarization. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18251508/ · DOI 10.1021/tx700204r
Complete structured claim and evidence
After 24 hours, both solutions caused necrotic cell death without significant caspase-3 activation; approximately 10 micromolar total V produced 50% viability loss.
Decavanadate(V) → Necrotic death in vanadate-exposed rat cardiomyocytes source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Neonatal rat ventricular cells; MTT and propidium iodide assays.
limitations
No clinical cardiac-risk estimate can be derived from the culture concentration.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The injury phenotype was necrotic in this experiment.
primary_references
Vanadate induces necrotic death in neonatal rat cardiomyocytes through mitochondrial membrane depolarization. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18251508/ · DOI 10.1021/tx700204r
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Neonatal rat ventricular cells; MTT and propidium iodide assays. · source_derived_draft · unverified_draft
## vanadium-cardiac-necrosis The injury phenotype was necrotic in this experiment. After 24 hours, both solutions caused necrotic cell death without significant caspase-3 activation; approximately 10 micromolar total V produced 50% viability loss. Model: Neonatal rat ventricular cells; MTT and propidium iodide assays. Limitations: No clinical cardiac-risk estimate can be derived from the culture concentration. Evidence access: Primary abstract Vanadate induces necrotic death in neonatal rat cardiomyocytes through mitochondrial membrane depolarization. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18251508/ · DOI 10.1021/tx700204r
Complete structured claim and evidence
Vanadate-treated rat cardiomyocytes showed sustained elevation of cytosolic calcium after 24 hours near the viability-loss concentrations.
Decavanadate(V) → Cytosolic calcium in vanadate-exposed rat cardiomyocytes source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Fura-2 imaging in neonatal rat cardiomyocytes.
limitations
Association does not identify whether SERCA, other transporters or secondary cell injury caused the calcium rise.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Ion regulation changed alongside mitochondrial injury.
primary_references
Vanadate induces necrotic death in neonatal rat cardiomyocytes through mitochondrial membrane depolarization. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18251508/ · DOI 10.1021/tx700204r
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 302–308
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Fura-2 imaging in neonatal rat cardiomyocytes. · source_derived_draft · unverified_draft
## vanadium-cardiac-calcium Ion regulation changed alongside mitochondrial injury. Vanadate-treated rat cardiomyocytes showed sustained elevation of cytosolic calcium after 24 hours near the viability-loss concentrations. Model: Fura-2 imaging in neonatal rat cardiomyocytes. Limitations: Association does not identify whether SERCA, other transporters or secondary cell injury caused the calcium rise. Evidence access: Primary abstract Vanadate induces necrotic death in neonatal rat cardiomyocytes through mitochondrial membrane depolarization. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18251508/ · DOI 10.1021/tx700204r
Complete structured claim and evidence
Decavanadate inhibited isolated Sparus aurata heart mitochondrial oxygen consumption more potently than monomeric vanadate in the reported assay.
Decavanadate(V) → Respiration of isolated Sparus aurata heart mitochondria source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Fish cardiac mitochondria; IC50 400 nM V10 versus 23 micromolar V1 as reported.
limitations
Species and concentration basis matter; compare ten V atoms per decamer before inferring a per-atom potency ratio.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Oligomeric form changed potency in an isolated organelle.
primary_references
Mitochondria as a target for decavanadate toxicity in Sparus aurata heart. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17420061/ · DOI 10.1016/j.aquatox.2007.03.005
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Fish cardiac mitochondria; IC50 400 nM V10 versus 23 micromolar V1 as reported. · source_derived_draft · unverified_draft
## vanadium-fish-decamer-potency Oligomeric form changed potency in an isolated organelle. Decavanadate inhibited isolated Sparus aurata heart mitochondrial oxygen consumption more potently than monomeric vanadate in the reported assay. Model: Fish cardiac mitochondria; IC50 400 nM V10 versus 23 micromolar V1 as reported. Limitations: Species and concentration basis matter; compare ten V atoms per decamer before inferring a per-atom potency ratio. Evidence access: Primary abstract Mitochondria as a target for decavanadate toxicity in Sparus aurata heart. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17420061/ · DOI 10.1016/j.aquatox.2007.03.005
Complete structured claim and evidence
Up to 5 micromolar V10 did not inhibit measured F0F1-ATPase activity, NADH levels or complexes I/II, while complex-III redox steady state changed.
Decavanadate(V) → Complex III redox state in fish cardiac mitochondria source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Isolated fish cardiac mitochondrial assays.
limitations
Complex-III redox change does not itself establish a direct molecular binding target.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Respiratory inhibition did not mean every mitochondrial enzyme was inhibited.
primary_references
Mitochondria as a target for decavanadate toxicity in Sparus aurata heart. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17420061/ · DOI 10.1016/j.aquatox.2007.03.005
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Isolated fish cardiac mitochondrial assays. · source_derived_draft · unverified_draft
## vanadium-fish-target-specificity Respiratory inhibition did not mean every mitochondrial enzyme was inhibited. Up to 5 micromolar V10 did not inhibit measured F0F1-ATPase activity, NADH levels or complexes I/II, while complex-III redox steady state changed. Model: Isolated fish cardiac mitochondrial assays. Limitations: Complex-III redox change does not itself establish a direct molecular binding target. Evidence access: Primary abstract Mitochondria as a target for decavanadate toxicity in Sparus aurata heart. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17420061/ · DOI 10.1016/j.aquatox.2007.03.005
Complete structured claim and evidence
Vanadate increased NO release above 50 micromolar in the tested rat UMR106 and mouse MC3T3-E1 osteoblast-like cultures, with a biphasic concentration response.
Vanadate(V), protonation/speciation dependent → NO production in vanadate-exposed osteoblast-like cells source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rodent osteoblast-like cell cultures; 2.5–100 micromolar vanadate.
limitations
Mixed cell models are named explicitly; NO is a proposed mediator, not proven sole cause of growth effects.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A growth-related exposure can engage nitrosative signaling at higher concentrations.
primary_references
Vanadate-induced nitric oxide production: role in osteoblast growth and differentiation. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10988345/ · DOI 10.1016/s0014-2999(00)00356-3
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rodent osteoblast-like cell cultures; 2.5–100 micromolar vanadate. · source_derived_draft · unverified_draft
## vanadium-bone-no A growth-related exposure can engage nitrosative signaling at higher concentrations. Vanadate increased NO release above 50 micromolar in the tested rat UMR106 and mouse MC3T3-E1 osteoblast-like cultures, with a biphasic concentration response. Model: Rodent osteoblast-like cell cultures; 2.5–100 micromolar vanadate. Limitations: Mixed cell models are named explicitly; NO is a proposed mediator, not proven sole cause of growth effects. Evidence access: Primary abstract Vanadate-induced nitric oxide production: role in osteoblast growth and differentiation. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10988345/ · DOI 10.1016/s0014-2999(00)00356-3
Complete structured claim and evidence
The NO donor sodium nitroprusside reduced growth and alkaline-phosphatase activity, mimicking part of the vanadate phenotype.
Sodium nitroprusside → Growth and alkaline-phosphatase activity in rodent osteoblast-like cells source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Rat UMR106 and mouse MC3T3-E1 culture program.
limitations
Mimicry is not equivalent to selective blockade and rescue of the proposed vanadate mechanism.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A donor experiment supports a possible downstream mediator.
primary_references
Vanadate-induced nitric oxide production: role in osteoblast growth and differentiation. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10988345/ · DOI 10.1016/s0014-2999(00)00356-3
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat UMR106 and mouse MC3T3-E1 culture program. · source_derived_draft · unverified_draft
## vanadium-bone-no-donor A donor experiment supports a possible downstream mediator. The NO donor sodium nitroprusside reduced growth and alkaline-phosphatase activity, mimicking part of the vanadate phenotype. Model: Rat UMR106 and mouse MC3T3-E1 culture program. Limitations: Mimicry is not equivalent to selective blockade and rescue of the proposed vanadate mechanism. Evidence access: Primary abstract Vanadate-induced nitric oxide production: role in osteoblast growth and differentiation. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10988345/ · DOI 10.1016/s0014-2999(00)00356-3
Complete structured claim and evidence
The rat study reported that berberine plus vanadyl acetylacetonate reduced hyperglycemia and improved vascular calcification, junction and barrier outcomes compared with single-agent conditions.
Berberine → Bis(acetylacetonato)oxovanadium(IV) source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Diabetic rats; primary abstract accessed.
limitations
Preclinical formulation-specific findings; doses and formal synergy modeling are not resolved in accessed abstract. Not a recommendation to combine supplements.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A specific tested combination is recorded rather than inferred from a shared pathway.
primary_references
Vanadyl Acetylacetonate and Berberine Synergistically Ameliorate Diabetes-induced Vascular Dysfunction and Reduce Endothelial Toxicity through ERK and Akt Regulation. · 2026 · https://pubmed.ncbi.nlm.nih.gov/40775562/ · DOI 10.1007/s12011-025-04774-z
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Diabetic rats; primary abstract accessed. · source_derived_draft · unverified_draft
## vanadium-berberine-vascular-combination A specific tested combination is recorded rather than inferred from a shared pathway. The rat study reported that berberine plus vanadyl acetylacetonate reduced hyperglycemia and improved vascular calcification, junction and barrier outcomes compared with single-agent conditions. Model: Diabetic rats; primary abstract accessed. Limitations: Preclinical formulation-specific findings; doses and formal synergy modeling are not resolved in accessed abstract. Not a recommendation to combine supplements. Evidence access: Primary abstract Vanadyl Acetylacetonate and Berberine Synergistically Ameliorate Diabetes-induced Vascular Dysfunction and Reduce Endothelial Toxicity through ERK and Akt Regulation. · 2026 · https://pubmed.ncbi.nlm.nih.gov/40775562/ · DOI 10.1007/s12011-025-04774-z
Complete structured claim and evidence
In HUVEC experiments, berberine reduced vanadyl-acetylacetonate-associated apoptosis, junction/cytoskeleton damage and permeability changes, with lower excessive ERK/Akt phosphorylation.
Berberine → Vanadyl-acetylacetonate injury in human HUVEC cultures source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human endothelial-cell experiments accompanying diabetic-rat study.
limitations
Pathway association does not establish direct inhibition of ERK or Akt by berberine at human exposure.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Protection from one compound’s cellular toxicity can accompany lower signaling activity.
primary_references
Vanadyl Acetylacetonate and Berberine Synergistically Ameliorate Diabetes-induced Vascular Dysfunction and Reduce Endothelial Toxicity through ERK and Akt Regulation. · 2026 · https://pubmed.ncbi.nlm.nih.gov/40775562/ · DOI 10.1007/s12011-025-04774-z
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human endothelial-cell experiments accompanying diabetic-rat study. · source_derived_draft · unverified_draft
## vanadium-berberine-endothelium Protection from one compound’s cellular toxicity can accompany lower signaling activity. In HUVEC experiments, berberine reduced vanadyl-acetylacetonate-associated apoptosis, junction/cytoskeleton damage and permeability changes, with lower excessive ERK/Akt phosphorylation. Model: Human endothelial-cell experiments accompanying diabetic-rat study. Limitations: Pathway association does not establish direct inhibition of ERK or Akt by berberine at human exposure. Evidence access: Primary abstract Vanadyl Acetylacetonate and Berberine Synergistically Ameliorate Diabetes-induced Vascular Dysfunction and Reduce Endothelial Toxicity through ERK and Akt Regulation. · 2026 · https://pubmed.ncbi.nlm.nih.gov/40775562/ · DOI 10.1007/s12011-025-04774-z
Complete structured claim and evidence
Dietary vanadium overexposure in ducks was associated with lower NADH/FSP1/CoQ10-axis measures and increased hepatic lipid peroxidation and Fe2+ accumulation.
Ammonium metavanadate → Duck FSP1 / AIFM2 source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text
experimental_model
Ammonium metavanadate diets reported as 30 or 45 mg V/kg feed; 42-day duck study.
limitations
Observational pathway measurements after exposure, not direct enzyme inhibition or a human ferroptosis mechanism. Methods inconsistently say three and four groups while listing control plus two exposure groups.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
An animal toxicity study links the exposure to a lipid-defense pathway.
primary_references
Dual-pathway mechanism of vanadium-induced hepatotoxicity in ducks: Synergistic crosstalk between glucose homeostasis disruption and NADH/FSP1/COQ10 axis-driven ferroptosis. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41362732/ · DOI 10.7150/ijbs.123482
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Ammonium metavanadate diets reported as 30 or 45 mg V/kg feed; 42-day duck study. · source_derived_draft · unverified_draft
## vanadium-duck-redox-axis An animal toxicity study links the exposure to a lipid-defense pathway. Dietary vanadium overexposure in ducks was associated with lower NADH/FSP1/CoQ10-axis measures and increased hepatic lipid peroxidation and Fe2+ accumulation. Model: Ammonium metavanadate diets reported as 30 or 45 mg V/kg feed; 42-day duck study. Limitations: Observational pathway measurements after exposure, not direct enzyme inhibition or a human ferroptosis mechanism. Methods inconsistently say three and four groups while listing control plus two exposure groups. Evidence access: Primary full text Dual-pathway mechanism of vanadium-induced hepatotoxicity in ducks: Synergistic crosstalk between glucose homeostasis disruption and NADH/FSP1/COQ10 axis-driven ferroptosis. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41362732/ · DOI 10.7150/ijbs.123482
Complete structured claim and evidence
Vanadium-exposed duck livers showed wider ER–mitochondrial gaps and altered abundance/association of the IP3R–GRP75–VDAC1 contact complex.
Ammonium metavanadate → Mitochondria–ER contacts in vanadium-exposed duck liver source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text
experimental_model
Duck liver ultrastructure and MAM proteomics/co-association measurements.
limitations
No genetic or inhibitor rescue establishing this chain was extracted. Human orthologues are not substituted for duck measurements.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A change at organelle contacts may link calcium handling, metabolism and injury.
primary_references
Dual-pathway mechanism of vanadium-induced hepatotoxicity in ducks: Synergistic crosstalk between glucose homeostasis disruption and NADH/FSP1/COQ10 axis-driven ferroptosis. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41362732/ · DOI 10.7150/ijbs.123482
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Duck liver ultrastructure and MAM proteomics/co-association measurements. · source_derived_draft · unverified_draft
## vanadium-duck-mam A change at organelle contacts may link calcium handling, metabolism and injury. Vanadium-exposed duck livers showed wider ER–mitochondrial gaps and altered abundance/association of the IP3R–GRP75–VDAC1 contact complex. Model: Duck liver ultrastructure and MAM proteomics/co-association measurements. Limitations: No genetic or inhibitor rescue establishing this chain was extracted. Human orthologues are not substituted for duck measurements. Evidence access: Primary full text Dual-pathway mechanism of vanadium-induced hepatotoxicity in ducks: Synergistic crosstalk between glucose homeostasis disruption and NADH/FSP1/COQ10 axis-driven ferroptosis. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41362732/ · DOI 10.7150/ijbs.123482
Complete structured claim and evidence
In the 16-person six-week type-2-diabetes trial, clamp glucose metabolism did not improve at 75 mg/day VOSO4; improvement occurred in three of five at 150 mg/day and four of eight at 300 mg/day.
Vanadyl sulfate → Clamp glucose disposal after vanadyl sulfate source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Small placebo-lead-in dose-ranging trial; doses are sulfate preparation mass.
limitations
Responder counts are not a demonstrated group-wide clinical benefit; later pharmacokinetic analysis uses the same cohort.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Some individuals responded while others did not.
primary_references
Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Small placebo-lead-in dose-ranging trial; doses are sulfate preparation mass. · source_derived_draft · unverified_draft
## vanadium-human-glucose-variable Some individuals responded while others did not. In the 16-person six-week type-2-diabetes trial, clamp glucose metabolism did not improve at 75 mg/day VOSO4; improvement occurred in three of five at 150 mg/day and four of eight at 300 mg/day. Model: Small placebo-lead-in dose-ranging trial; doses are sulfate preparation mass. Limitations: Responder counts are not a demonstrated group-wide clinical benefit; later pharmacokinetic analysis uses the same cohort. Evidence access: Primary abstract Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
Complete structured claim and evidence
Basal hepatic glucose production and its insulin suppression were unchanged at all three doses in the 16-person trial.
Vanadyl sulfate → Hepatic glucose production in the six-week vanadyl trial source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Same six-week type-2-diabetes dose-ranging study.
limitations
Different results in a smaller sequential study are retained with study design and dose, not automatically labeled contradiction.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A peripheral response did not imply improved liver insulin response.
primary_references
Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Same six-week type-2-diabetes dose-ranging study. · source_derived_draft · unverified_draft
## vanadium-human-hepatic-null A peripheral response did not imply improved liver insulin response. Basal hepatic glucose production and its insulin suppression were unchanged at all three doses in the 16-person trial. Model: Same six-week type-2-diabetes dose-ranging study. Limitations: Different results in a smaller sequential study are retained with study design and dose, not automatically labeled contradiction. Evidence access: Primary abstract Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
Complete structured claim and evidence
After vanadyl treatment, muscle showed trends toward increased basal insulin-receptor, IRS1 and Shc tyrosine phosphorylation and IRS1-associated PI3K activity without additional insulin-stimulated increases.
Vanadyl sulfate → Insulin receptor / INSR source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human muscle samples from the same 16-person trial.
limitations
Reported as trends; phosphorylation patterns did not clearly correlate with glucose disposal. No proven nutrient requirement.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Early signaling markers did not guarantee a larger response to insulin.
primary_references
Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human muscle samples from the same 16-person trial. · source_derived_draft · unverified_draft
## vanadium-human-signaling Early signaling markers did not guarantee a larger response to insulin. After vanadyl treatment, muscle showed trends toward increased basal insulin-receptor, IRS1 and Shc tyrosine phosphorylation and IRS1-associated PI3K activity without additional insulin-stimulated increases. Model: Human muscle samples from the same 16-person trial. Limitations: Reported as trends; phosphorylation patterns did not clearly correlate with glucose disposal. No proven nutrient requirement. Evidence access: Primary abstract Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
Complete structured claim and evidence
Vanadyl did not change basal or insulin-stimulated muscle glycogen-synthase activity in the six-week study.
Vanadyl sulfate → Muscle glycogen-synthase activity after vanadyl sulfate source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human muscle assay from the dose-ranging trial.
limitations
Assay result is not a full glycogen-flux measurement.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
A change in upstream signaling did not establish a change at every downstream enzyme.
primary_references
Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
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AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human muscle assay from the dose-ranging trial. · source_derived_draft · unverified_draft
## vanadium-human-glycogen-null A change in upstream signaling did not establish a change at every downstream enzyme. Vanadyl did not change basal or insulin-stimulated muscle glycogen-synthase activity in the six-week study. Model: Human muscle assay from the dose-ranging trial. Limitations: Assay result is not a full glycogen-flux measurement. Evidence access: Primary abstract Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
Complete structured claim and evidence
The 150- and 300-mg/day sulfate regimens caused some gastrointestinal intolerance during the six-week trial.
Vanadyl sulfate → Gastrointestinal intolerance during vanadyl sulfate studies source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Small human type-2-diabetes study.
limitations
Short follow-up and limited endpoints do not establish long-term safety.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Tolerability limits matter alongside the metabolic signals.
primary_references
Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 406–412
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Small human type-2-diabetes study. · source_derived_draft · unverified_draft
## vanadium-human-gi Tolerability limits matter alongside the metabolic signals. The 150- and 300-mg/day sulfate regimens caused some gastrointestinal intolerance during the six-week trial. Model: Small human type-2-diabetes study. Limitations: Short follow-up and limited endpoints do not establish long-term safety. Evidence access: Primary abstract Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10726921/ · DOI 10.1016/s0026-0495(00)90418-9
Complete structured claim and evidence
Total serum vanadium was not significantly correlated with insulin sensitivity in the pharmacokinetic analysis of the 16-person trial.
Total vanadium in human serum → Clamp glucose disposal after vanadyl sulfate source_derived_draftungraded
Experimental context and source evidence
availability_state
biomarker_context Imported condition classification; unverified.
evidence_access
Primary full text
experimental_model
Reanalysis of the same six-week vanadyl cohort; serum/blood/urine measurements.
limitations
Not independent efficacy replication; unmeasured tissue pools remain a hypothesis.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Total circulating metal is not a reliable proxy for the active tissue species.
primary_references
Coordination chemistry may explain pharmacokinetics and clinical response of vanadyl sulfate in type 2 diabetic patients. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23982218/ · DOI 10.1039/c3mt00162h
trigger_kind
biomarker_context Imported condition classification; unverified.
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 414–420
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reanalysis of the same six-week vanadyl cohort; serum/blood/urine measurements. · source_derived_draft · unverified_draft
## vanadium-human-serum-marker Total circulating metal is not a reliable proxy for the active tissue species. Total serum vanadium was not significantly correlated with insulin sensitivity in the pharmacokinetic analysis of the 16-person trial. Model: Reanalysis of the same six-week vanadyl cohort; serum/blood/urine measurements. Limitations: Not independent efficacy replication; unmeasured tissue pools remain a hypothesis. Evidence access: Primary full text Coordination chemistry may explain pharmacokinetics and clinical response of vanadyl sulfate in type 2 diabetic patients. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23982218/ · DOI 10.1039/c3mt00162h
Complete structured claim and evidence
The fitted serum elimination half-times averaged about 4.7 and 4.6 days in the 50- and 100-mg elemental-V/day groups.
Vanadyl sulfate → Serum vanadium elimination after sulfate exposure source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text
experimental_model
Same cohort; one-compartment first-order model.
limitations
Elemental V amounts differ from sulfate mass; fitted serum kinetics are not every tissue’s clearance.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Metal handling continues beyond the last swallowed dose.
primary_references
Coordination chemistry may explain pharmacokinetics and clinical response of vanadyl sulfate in type 2 diabetic patients. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23982218/ · DOI 10.1039/c3mt00162h
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 422–428
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Same cohort; one-compartment first-order model. · source_derived_draft · unverified_draft
## vanadium-human-excretion Metal handling continues beyond the last swallowed dose. The fitted serum elimination half-times averaged about 4.7 and 4.6 days in the 50- and 100-mg elemental-V/day groups. Model: Same cohort; one-compartment first-order model. Limitations: Elemental V amounts differ from sulfate mass; fitted serum kinetics are not every tissue’s clearance. Evidence access: Primary full text Coordination chemistry may explain pharmacokinetics and clinical response of vanadyl sulfate in type 2 diabetic patients. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23982218/ · DOI 10.1039/c3mt00162h
Complete structured claim and evidence
Daily urinary recovery was roughly 1% or less of administered elemental V in the trial, used by the authors to estimate low oral absorption.
Vanadyl sulfate → Urinary recovery of orally administered vanadium source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary full text
experimental_model
Same cohort; steady-state urine measurements.
limitations
The full text calls this a minimum absorption estimate because tissue accumulation and other compartments can matter; do not present it as complete mass balance.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Only a small fraction of the oral dose appeared in urine each day.
primary_references
Coordination chemistry may explain pharmacokinetics and clinical response of vanadyl sulfate in type 2 diabetic patients. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23982218/ · DOI 10.1039/c3mt00162h
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 430–436
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Same cohort; steady-state urine measurements. · source_derived_draft · unverified_draft
## vanadium-human-absorption-estimate Only a small fraction of the oral dose appeared in urine each day. Daily urinary recovery was roughly 1% or less of administered elemental V in the trial, used by the authors to estimate low oral absorption. Model: Same cohort; steady-state urine measurements. Limitations: The full text calls this a minimum absorption estimate because tissue accumulation and other compartments can matter; do not present it as complete mass balance. Evidence access: Primary full text Coordination chemistry may explain pharmacokinetics and clinical response of vanadyl sulfate in type 2 diabetic patients. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23982218/ · DOI 10.1039/c3mt00162h
Complete structured claim and evidence
In eight patients given 50 mg vanadyl sulfate twice daily for four weeks, fasting glucose and hepatic glucose output during insulin infusion decreased, without significant whole-body glucose-uptake improvement.
Vanadyl sulfate → Insulin-suppressed hepatic glucose output after four weeks of vanadyl source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Single-blind sequential study; six patients continued to a subsequent placebo phase.
limitations
Fixed treatment order and persistence into placebo complicate causal inference; six of eight had early gastrointestinal effects.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
Another small study found a liver-associated effect rather than broad uptake improvement.
primary_references
Effects of vanadyl sulfate on carbohydrate and lipid metabolism in patients with non-insulin-dependent diabetes mellitus. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8781301/ · DOI 10.1016/s0026-0495(96)90013-x
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 438–444
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Single-blind sequential study; six patients continued to a subsequent placebo phase. · source_derived_draft · unverified_draft
## vanadium-human-small-hepatic-positive Another small study found a liver-associated effect rather than broad uptake improvement. In eight patients given 50 mg vanadyl sulfate twice daily for four weeks, fasting glucose and hepatic glucose output during insulin infusion decreased, without significant whole-body glucose-uptake improvement. Model: Single-blind sequential study; six patients continued to a subsequent placebo phase. Limitations: Fixed treatment order and persistence into placebo complicate causal inference; six of eight had early gastrointestinal effects. Evidence access: Primary abstract Effects of vanadyl sulfate on carbohydrate and lipid metabolism in patients with non-insulin-dependent diabetes mellitus. · 1996 · https://pubmed.ncbi.nlm.nih.gov/8781301/ · DOI 10.1016/s0026-0495(96)90013-x
Complete structured claim and evidence
Seven healthy active adults showed no improvement in fasting glucose, fasting insulin or OGTT-derived insulin-sensitivity index after one or seven days of vanadyl sulfate.
Vanadyl sulfate → Insulin sensitivity in healthy active adults after vanadyl source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
One hundred mg before acute testing, then 50 mg twice daily for six days; within-person design.
limitations
Small short study without a randomized placebo comparator; not proof of no effect at every exposure.
nutrient_topic
Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
plain_language
The small healthy-volunteer study did not show the hoped-for insulin benefit.
primary_references
Effect of acute and short-term administration of vanadyl sulphate on insulin sensitivity in healthy active humans. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12500990/ · DOI 10.1123/ijsnem.12.4.470
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 446–452
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · One hundred mg before acute testing, then 50 mg twice daily for six days; within-person design. · source_derived_draft · unverified_draft
## vanadium-healthy-null The small healthy-volunteer study did not show the hoped-for insulin benefit. Seven healthy active adults showed no improvement in fasting glucose, fasting insulin or OGTT-derived insulin-sensitivity index after one or seven days of vanadyl sulfate. Model: One hundred mg before acute testing, then 50 mg twice daily for six days; within-person design. Limitations: Small short study without a randomized placebo comparator; not proof of no effect at every exposure. Evidence access: Primary abstract Effect of acute and short-term administration of vanadyl sulphate on insulin sensitivity in healthy active humans. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12500990/ · DOI 10.1123/ijsnem.12.4.470
Complete structured claim and evidence
The transferrin-cycle model supported by the binding experiments releases iron in acidified endosomes while apotransferrin remains receptor-bound.
Human serum transferrin / TF → Transferrin-dependent endosomal iron delivery to cytosol source_derived_draftungraded
Experimental context and source evidence
evidence_span
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experimental_model
Receptor binding at controlled pH and transferrin cycle analysis
exposure
Apotransferrin and diferric transferrin binding at acidic versus neutral pH
limitations
The indexed abstract does not identify the cell line; its experiments support a pH-dependent trafficking model, not direct measures of whole-body iron turnover.
nutrient_topic
Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
organism
Cultured-cell transferrin receptor system
plain_language
The carrier gives up its iron inside an acidic compartment but stays attached to its return transport.
primary_references
[iron-p6300903] pH and the recycling of transferrin during receptor-mediated endocytosis. (1983). https://pubmed.ncbi.nlm.nih.gov/6300903/ DOI: 10.1073/pnas.80.8.2258
tissue_or_cell_type
Cell surface and endosomal recycling model
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 420–431
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Receptor binding at controlled pH and transferrin cycle analysis · source_derived_draft · unverified_draft
### iron-tf-acidic-release The transferrin-cycle model supported by the binding experiments releases iron in acidified endosomes while apotransferrin remains receptor-bound. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The carrier gives up its iron inside an acidic compartment but stays attached to its return transport. organism: Cultured-cell transferrin receptor system tissue_or_cell_type: Cell surface and endosomal recycling model experimental_model: Receptor binding at controlled pH and transferrin cycle analysis limitations: The indexed abstract does not identify the cell line; its experiments support a pH-dependent trafficking model, not direct measures of whole-body iron turnover. exposure: Apotransferrin and diferric transferrin binding at acidic versus neutral pH evidence_span: {"source_cache": "artifacts/iron-research/6300903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852", "start_char": 0, "end_char": 906, "text_sha256": "29d23cdaaacd30003c1f3e70935d7ab5ccbb1612379d6e650d356d1235438852"} [iron-p6300903] pH and the recycling of transferrin during receptor-mediated endocytosis. (1983). https://pubmed.ncbi.nlm.nih.gov/6300903/ DOI: 10.1073/pnas.80.8.2258
Complete structured claim and evidence
Steap3 colocalized with transferrin-cycle endosomes and promoted iron reduction and transferrin-dependent iron uptake.
Mouse metalloreductase Steap3 → Transferrin-dependent endosomal iron delivery to cytosol source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/iron-research/16227996.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cd6e35b6ea534163d0db76cbdec2fa6c3c2dd998b0a1f66d9f16479bcb87711b", "start_char": 0, "end_char": 1006, "text_sha256": "cd6e35b6ea534163d0db76cbdec2fa6c3c2dd998b0a1f66d9f16479bcb87711b"}
experimental_model
Positional cloning, overexpression and deficient-mouse experiments
exposure
Steap3 deficiency and overexpression
limitations
A dominant erythroid reduction pathway, not proof of equal dependence in every tissue.
nutrient_topic
Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
organism
Mice and mouse Steap3 expression systems
plain_language
Iron released from transferrin needs another chemical reduction step before it can leave the endosome.
primary_references
[iron-p16227996] Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. (2005). https://pubmed.ncbi.nlm.nih.gov/16227996/ DOI: 10.1038/ng1658
tissue_or_cell_type
Erythroid endosomes
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 446–457
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Positional cloning, overexpression and deficient-mouse experiments · source_derived_draft · unverified_draft
### iron-steap-reduction Steap3 colocalized with transferrin-cycle endosomes and promoted iron reduction and transferrin-dependent iron uptake. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron released from transferrin needs another chemical reduction step before it can leave the endosome. organism: Mice and mouse Steap3 expression systems tissue_or_cell_type: Erythroid endosomes experimental_model: Positional cloning, overexpression and deficient-mouse experiments limitations: A dominant erythroid reduction pathway, not proof of equal dependence in every tissue. exposure: Steap3 deficiency and overexpression evidence_span: {"source_cache": "artifacts/iron-research/16227996.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cd6e35b6ea534163d0db76cbdec2fa6c3c2dd998b0a1f66d9f16479bcb87711b", "start_char": 0, "end_char": 1006, "text_sha256": "cd6e35b6ea534163d0db76cbdec2fa6c3c2dd998b0a1f66d9f16479bcb87711b"} [iron-p16227996] Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. (2005). https://pubmed.ncbi.nlm.nih.gov/16227996/ DOI: 10.1038/ng1658
Complete structured claim and evidence
FSP1 used NAD(P)H to regenerate the reduced CoQ pool that traps lipid peroxyl radicals.
NADPH → FSP1 / AIFM2 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/31634899.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1e96f6d5aed6def29533d907cd9ae90bc287d3f7beb6b9447aec3308d57a0dfe", "start_char": 0, "end_char": 1818, "text_sha256": "1e96f6d5aed6def29533d907cd9ae90bc287d3f7beb6b9447aec3308d57a0dfe"}
experimental_model
Expression cloning and cell-death experiments
exposure
GPX4 deletion or inhibitors and FSP1 manipulation
limitations
Cancer-cell defense mechanism; preventing ferroptosis is not always a desirable disease outcome and oral CoQ benefit is not tested.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Human cancer-cell models
plain_language
The antioxidant form must be regenerated using reducing power.
primary_references
[coq10-p31634899] FSP1 is a glutathione-independent ferroptosis suppressor. (2019). https://pubmed.ncbi.nlm.nih.gov/31634899/ DOI: 10.1038/s41586-019-1707-0
tissue_or_cell_type
FSP1-CoQ antioxidant pathway
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 801–812
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Expression cloning and cell-death experiments · source_derived_draft · unverified_draft
### coq10-fsp1-nadph FSP1 used NAD(P)H to regenerate the reduced CoQ pool that traps lipid peroxyl radicals. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The antioxidant form must be regenerated using reducing power. organism: Human cancer-cell models tissue_or_cell_type: FSP1-CoQ antioxidant pathway experimental_model: Expression cloning and cell-death experiments limitations: Cancer-cell defense mechanism; preventing ferroptosis is not always a desirable disease outcome and oral CoQ benefit is not tested. exposure: GPX4 deletion or inhibitors and FSP1 manipulation evidence_span: {"source_cache": "artifacts/coq10-research/31634899.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1e96f6d5aed6def29533d907cd9ae90bc287d3f7beb6b9447aec3308d57a0dfe", "start_char": 0, "end_char": 1818, "text_sha256": "1e96f6d5aed6def29533d907cd9ae90bc287d3f7beb6b9447aec3308d57a0dfe"} [coq10-p31634899] FSP1 is a glutathione-independent ferroptosis suppressor. (2019). https://pubmed.ncbi.nlm.nih.gov/31634899/ DOI: 10.1038/s41586-019-1707-0
Complete structured claim and evidence
Lipoic acid reduced phosphatase activity and PTP1B thiol reactivity in 3T3-L1 cells.
Lipoic acid → Mouse protein tyrosine phosphatase 1B / Ptpn1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/ala-research/12948866.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0440cb8edaf0213af3824367ee799d1a1916ed2340c9da99588d83c7581804b9", "start_char": 0, "end_char": 1489, "text_sha256": "0440cb8edaf0213af3824367ee799d1a1916ed2340c9da99588d83c7581804b9"}
experimental_model
Protein-thiol, phosphorylation and glucose-uptake assays
exposure
Alpha-lipoic-acid stimulation with redox/thiol inhibitors
limitations
Cell-culture redox signaling; not proof that lipoic acid invariably lowers oxidation in all settings.
nutrient_topic
Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
organism
Mouse
plain_language
The exposure weakened a phosphatase brake on phosphorylation signaling.
primary_references
[ala-p12948866] Alpha-lipoic acid decreases thiol reactivity of the insulin receptor and protein tyrosine phosphatase 1B in 3T3-L1 adipocytes. (2003). https://pubmed.ncbi.nlm.nih.gov/12948866/ DOI: 10.1016/s0006-2952(03)00395-2
tissue_or_cell_type
3T3-L1 adipocytes
Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 949–960
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein-thiol, phosphorylation and glucose-uptake assays · source_derived_draft · unverified_draft
### ala-adipocyte-ptp1b Lipoic acid reduced phosphatase activity and PTP1B thiol reactivity in 3T3-L1 cells. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The exposure weakened a phosphatase brake on phosphorylation signaling. organism: Mouse tissue_or_cell_type: 3T3-L1 adipocytes experimental_model: Protein-thiol, phosphorylation and glucose-uptake assays limitations: Cell-culture redox signaling; not proof that lipoic acid invariably lowers oxidation in all settings. exposure: Alpha-lipoic-acid stimulation with redox/thiol inhibitors evidence_span: {"source_cache": "artifacts/ala-research/12948866.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0440cb8edaf0213af3824367ee799d1a1916ed2340c9da99588d83c7581804b9", "start_char": 0, "end_char": 1489, "text_sha256": "0440cb8edaf0213af3824367ee799d1a1916ed2340c9da99588d83c7581804b9"} [ala-p12948866] Alpha-lipoic acid decreases thiol reactivity of the insulin receptor and protein tyrosine phosphatase 1B in 3T3-L1 adipocytes. (2003). https://pubmed.ncbi.nlm.nih.gov/12948866/ DOI: 10.1016/s0006-2952(03)00395-2
Complete structured claim and evidence
Obese rats receiving chromium picolinate had lower muscle PTP1B abundance and lower activity after correction for protein content.
Chromium(III) picolinate / CrPic → Rat protein tyrosine phosphatase 1B / Ptpn1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/chromium-research/16424121.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b0fa1d0917ec9cf4f3d309f2e9eb0e2b498e083ed1ff881b8f8df94a3cbe8119", "start_char": 0, "end_char": 1734, "text_sha256": "b0fa1d0917ec9cf4f3d309f2e9eb0e2b498e083ed1ff881b8f8df94a3cbe8119"}
experimental_model
Three-month supplementation and acute muscle insulin-signaling experiment
exposure
Chromium picolinate supplying approximately 80 µg Cr/kg/day; small obese and lean treatment groups
limitations
Model-specific supplementation. Lower phosphatase protein and activity do not prove direct chromium binding to PTP1B. Different results from cultured adipocytes are contextual, not a reason to erase either study.
nutrient_topic
Chromium research collection; topical membership is not evidence of a direct dietary effect. · Chromium
organism
Male JCR:LA-cp obese and lean rats
plain_language
A protein that can oppose insulin signaling was reduced in this rat model.
primary_references
[chromium-p16424121] Chromium picolinate enhances skeletal muscle cellular insulin signaling in vivo in obese, insulin-resistant JCR:LA-cp rats. (2006). https://pubmed.ncbi.nlm.nih.gov/16424121/ DOI: 10.1093/jn/136.2.415
tissue_or_cell_type
Vastus lateralis skeletal muscle
Chromium: transport, insulin signaling, nutrient interactions and essentiality debate (2026-09-17) · lines 445–456
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Three-month supplementation and acute muscle insulin-signaling experiment · source_derived_draft · unverified_draft
### chromium-rat-ptp1b-response Obese rats receiving chromium picolinate had lower muscle PTP1B abundance and lower activity after correction for protein content. Condition category: normal nutrient_topic: Chromium research collection; topical membership is not evidence of a direct dietary effect. plain_language: A protein that can oppose insulin signaling was reduced in this rat model. organism: Male JCR:LA-cp obese and lean rats tissue_or_cell_type: Vastus lateralis skeletal muscle experimental_model: Three-month supplementation and acute muscle insulin-signaling experiment limitations: Model-specific supplementation. Lower phosphatase protein and activity do not prove direct chromium binding to PTP1B. Different results from cultured adipocytes are contextual, not a reason to erase either study. exposure: Chromium picolinate supplying approximately 80 µg Cr/kg/day; small obese and lean treatment groups evidence_span: {"source_cache": "artifacts/chromium-research/16424121.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b0fa1d0917ec9cf4f3d309f2e9eb0e2b498e083ed1ff881b8f8df94a3cbe8119", "start_char": 0, "end_char": 1734, "text_sha256": "b0fa1d0917ec9cf4f3d309f2e9eb0e2b498e083ed1ff881b8f8df94a3cbe8119"} [chromium-p16424121] Chromium picolinate enhances skeletal muscle cellular insulin signaling in vivo in obese, insulin-resistant JCR:LA-cp rats. (2006). https://pubmed.ncbi.nlm.nih.gov/16424121/ DOI: 10.1093/jn/136.2.415
Complete structured claim and evidence
CGA showed noncompetitive PTP1B inhibition in the combined kinetic and NMR investigation.
Chlorogenic acid / 5-O-caffeoylquinic acid → PTP1B preparation in 2017 inhibition study, species not resolved from abstract source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/chlorogenic_acid-research/27959494.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4f4610d35c42975e3cc1026d2daa4014952bc442a58e711b430db873d22a7475", "start_char": 0, "end_char": 1044, "text_sha256": "4f4610d35c42975e3cc1026d2daa4014952bc442a58e711b430db873d22a7475"}
experimental_model
Steady-state kinetics, solution NMR and molecular dynamics
exposure
CGA compared with cichoric acid; quantitative assay regimen not given in abstract
limitations
Do not merge species-unresolved preparation with human or rodent PTPN1. An enzyme assay does not establish clinical insulin sensitization; simulated hydrogen-bond changes are a proposed mechanism.
nutrient_topic
Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. · Chlorogenic acid / 5-O-caffeoylquinic acid
organism
Purified PTP1B preparation; species not specified in indexed abstract
plain_language
An insulin-pathway regulator is a biochemical target candidate.
primary_references
[chlorogenic_acid-p27959494] Characterization of Protein Tyrosine Phosphatase 1B Inhibition by Chlorogenic Acid and Cichoric Acid. (2017). https://pubmed.ncbi.nlm.nih.gov/27959494/ DOI: 10.1021/acs.biochem.6b01025
tissue_or_cell_type
Enzyme inhibition and binding-site analysis
Chlorogenic acid: metabolism, signaling and nutrient connections (2026-09-17) · lines 516–527
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Steady-state kinetics, solution NMR and molecular dynamics · source_derived_draft · unverified_draft
### chlorogenic_acid-ptp1b-inhibition CGA showed noncompetitive PTP1B inhibition in the combined kinetic and NMR investigation. Condition category: normal nutrient_topic: Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: An insulin-pathway regulator is a biochemical target candidate. organism: Purified PTP1B preparation; species not specified in indexed abstract tissue_or_cell_type: Enzyme inhibition and binding-site analysis experimental_model: Steady-state kinetics, solution NMR and molecular dynamics limitations: Do not merge species-unresolved preparation with human or rodent PTPN1. An enzyme assay does not establish clinical insulin sensitization; simulated hydrogen-bond changes are a proposed mechanism. exposure: CGA compared with cichoric acid; quantitative assay regimen not given in abstract evidence_span: {"source_cache": "artifacts/chlorogenic_acid-research/27959494.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4f4610d35c42975e3cc1026d2daa4014952bc442a58e711b430db873d22a7475", "start_char": 0, "end_char": 1044, "text_sha256": "4f4610d35c42975e3cc1026d2daa4014952bc442a58e711b430db873d22a7475"} [chlorogenic_acid-p27959494] Characterization of Protein Tyrosine Phosphatase 1B Inhibition by Chlorogenic Acid and Cichoric Acid. (2017). https://pubmed.ncbi.nlm.nih.gov/27959494/ DOI: 10.1021/acs.biochem.6b01025
Complete structured claim and evidence
Hippocampal neuronal-specific PTP1B deletion prevented olanzapine-induced synaptic and cognitive deficits in mice.
Mouse protein tyrosine phosphatase 1B / Ptpn1 → Mouse cognitive/synaptic response during antipsychotic exposure source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_access
Primary abstract
experimental_model
Cell-type-specific mouse genetic intervention.
limitations
Does not mean ergothioneine reproduces every consequence of genetic deletion.
nutrient_topic
Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
plain_language
Removing the proposed target tested its role in the injury pathway.
primary_references
Gut microbiota-derived ergothioneine alleviates antipsychotic-induced synaptic and cognitive impairments. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42013837/ · DOI 10.1016/j.chom.2026.03.020
trigger_kind
machinery_impairment Imported condition classification; unverified.
Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 448–454
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-type-specific mouse genetic intervention. · source_derived_draft · unverified_draft
## ergothioneine-mouse-ptp1b-deletion Removing the proposed target tested its role in the injury pathway. Hippocampal neuronal-specific PTP1B deletion prevented olanzapine-induced synaptic and cognitive deficits in mice. Model: Cell-type-specific mouse genetic intervention. Limitations: Does not mean ergothioneine reproduces every consequence of genetic deletion. Evidence access: Primary abstract Gut microbiota-derived ergothioneine alleviates antipsychotic-induced synaptic and cognitive impairments. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42013837/ · DOI 10.1016/j.chom.2026.03.020
Complete structured claim and evidence

Availability and dependencies

Each situation shows the normal role first, then what the sources report under a specific condition. A shortfall in the diet, a fault in the machinery, and a low blood reading are kept separate because they are not the same thing.

An intact actin network gates glucose transport

Condition: machinery_impairment · Cytochalasin D disrupts actin in rat muscle cells.

Normal role: Transport and signaling depend on intact cellular machinery and local chemical species.

Recorded consequence: Transport stimulation is lost even when phosphatases are inhibited.

Scope: Species, dose, chemical preparation and assay remain on the linked records.

Transport inhibition changes thiol loss

Condition: machinery_impairment · DIDS treatment of human erythrocytes.

Normal role: Transport and signaling depend on intact cellular machinery and local chemical species.

Recorded consequence: Vanadate-associated intracellular/extracellular thiol shifts are attenuated.

Scope: Species, dose, chemical preparation and assay remain on the linked records.

Exporter activity contributes to glutathione efflux

Condition: machinery_impairment · MK571 treatment of erythrocytes.

Normal role: Transport and signaling depend on intact cellular machinery and local chemical species.

Recorded consequence: Glutathione efflux falls; transporter isoform remains unresolved.

Scope: Species, dose, chemical preparation and assay remain on the linked records.

Serum total metal does not predict the response

Condition: biomarker_context · Measurement of serum total V during a pharmacological trial.

Normal role: Transport and signaling depend on intact cellular machinery and local chemical species.

Recorded consequence: Total concentration does not reliably predict clamp insulin sensitivity.

Scope: Species, dose, chemical preparation and assay remain on the linked records.

The sources

Every document behind this chapter is preserved word for word. Open one to read it in full with its recorded conflicts marked in place.

Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Chlorogenic acid: metabolism, signaling and nutrient connections (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Chromium: transport, insulin signaling, nutrient interactions and essentiality debate (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19)AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · unverified_draftRead preserved source
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19)AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · unverified_draftRead preserved source

Recorded disagreements

Where two sources say different things, both are kept and the difference is explained. You can discuss a disagreement or propose a mechanism that might account for it.

Open questions in this collection

Questions the curators could not answer from the sources in front of them, kept here with the reason each one is still open. These are gaps in this collection, not findings or proof that no one has studied them.

Chapters are assembled from supplied drafts and curated literature summaries. Statements remain unverified against the primary studies, and the ledger is not medical advice.

Evidence, AI assistance and curation standards

Vanadium

The mechanisms

Vanadate competitively inhibited PTP1B with a reported Ki of 0.38 ± 0.02 micromolar.

Adding EDTA immediately and completely reversed vanadate inhibition of PTP1B in the assay.

Pervanadate irreversibly inhibited PTP1B by oxidation of its catalytic cysteine, supported by mass spectrometry.

Dithiothreitol rapidly converted pervanadate to vanadate under the phosphatase assay conditions.

Catalase blocked the slow time-dependent inactivation seen under some vanadate conditions, supporting an in-situ peroxide/pervanadate contribution.

Vanadate and pervanadate stimulated glucose transport and GLUT movement to the plasma membrane in rat L6 myotubes.

Wortmannin inhibited measured PI3K signaling but did not block vanadate/pervanadate-stimulated glucose transport; it did block insulin-stimulated transport.

Vanadate at concentrations that maximally stimulated glucose transport did not significantly increase Akt activity, whereas pervanadate and insulin did.

Cytochalasin D-mediated actin disassembly blocked glucose-transport stimulation by vanadate, pervanadate and insulin.

PKC inhibition or downregulation, alone or combined with wortmannin, failed to block vanadate/pervanadate-stimulated glucose transport.

Ascorbate generated V(IV) from vanadate in phosphate buffer at pH 7.4, but not comparably in water or the tested cacodylate buffer.

In phosphate/ascorbate mixtures with peroxide, reduced vanadium supported hydroxyl-radical generation; omitting phosphate sharply reduced the yield.

V(IV) generated by ascorbate/vanadate chemistry produced hydroperoxide-derived radicals from cumene hydroperoxide.

A vanadate/ascorbate/phosphate system oxidized NADH, with similar results for NADPH, through a proposed superoxide-initiated chain reaction.

Superoxide dismutase inhibited NADH oxidation in the vanadate/ascorbate/phosphate system, whereas catalase and ethanol did not.

Ascorbate initiated NADH oxidation at lower concentrations but inhibited it at higher concentrations in the same chemical system.

Glutathione and catalase reversed vanadate sensitivity in the susceptible cell line studied.

NADPH sensitized vanadate-resistant cells and increased phosphotyrosine signals and Ras expression in the reported experiment.

Vanadate exposure depleted intracellular nonprotein sulfhydryls while increasing extracellular glutathione in human erythrocytes.

DIDS inhibited the intracellular thiol decrease and extracellular increase during vanadate exposure, supporting an anion-transport-dependent step.

MK571 reduced glutathione efflux during erythrocyte vanadate exposure, suggesting involvement of an MRP-family exporter.

DMSA treatment of erythrocyte supernatants increased measured glutathione, consistent with release from metal-associated forms.

V(V) and V(IV) bound vacant transferrin iron-binding sites in culture medium even with a 20-fold molar excess of albumin, without displacing already-bound Fe(III) under those conditions.

Transferrin binding reduced vanadium uptake and antiproliferative activity in human A549 cells.

Vanadium binding did not increase transferrin affinity for TfR1 at pH 7.4, but disrupted conformational changes at pH 5.6 with citrate in the transferrin-cycle model.

Crystals of C-lobe-ferric human transferrin exposed to vanadyl acetylacetonate contained a two-vanadium(V) unit linked to Tyr188 rather than intact V(IV) acetylacetonate.

The vanadium adduct retained an open N-lobe and closed iron-containing C-lobe with little overall structural change.

Replacing 3 mM MgCl2 with MnCl2 lowered vanadate-binding Kd from 96 to 12 nM in the dog-kidney Na/K-ATPase preparation without changing binding capacity.

In magnesium-containing medium, potassium increased vanadate binding and lowered its Kd to about 11 nM without changing maximum binding.

Sodium decreased vanadate binding in magnesium-containing medium, whereas sodium and potassium had little effect in the manganese condition.

Vanadate occupied the catalytic site of calcium-free SERCA as planar VO3 with water and magnesium in a dephosphorylation-transition-like conformation.

Vanadate crystallization of rat-liver F1 ATP synthase captured an ADP–vanadate–Mg transition-like state with remodeling of the catalytic P-loop region.

In the vanadate-inhibited human ARSB structure, vanadate replaced sulfate at the active site and was covalently linked to the modified catalytic residue.

Human ARSB crystallography identified calcium coordinated in the sulfate-containing catalytic site and an essential modified Cys91 residue.

Decavanadate and mixed metavanadate solutions depolarized mitochondria in neonatal rat cardiomyocytes within six hours; half-maximal depolarization occurred near 6.5 micromolar total vanadium.

After 24 hours, both solutions caused necrotic cell death without significant caspase-3 activation; approximately 10 micromolar total V produced 50% viability loss.

Vanadate-treated rat cardiomyocytes showed sustained elevation of cytosolic calcium after 24 hours near the viability-loss concentrations.

Decavanadate inhibited isolated Sparus aurata heart mitochondrial oxygen consumption more potently than monomeric vanadate in the reported assay.

Up to 5 micromolar V10 did not inhibit measured F0F1-ATPase activity, NADH levels or complexes I/II, while complex-III redox steady state changed.

Vanadate increased NO release above 50 micromolar in the tested rat UMR106 and mouse MC3T3-E1 osteoblast-like cultures, with a biphasic concentration response.

The NO donor sodium nitroprusside reduced growth and alkaline-phosphatase activity, mimicking part of the vanadate phenotype.

The rat study reported that berberine plus vanadyl acetylacetonate reduced hyperglycemia and improved vascular calcification, junction and barrier outcomes compared with single-agent conditions.

In HUVEC experiments, berberine reduced vanadyl-acetylacetonate-associated apoptosis, junction/cytoskeleton damage and permeability changes, with lower excessive ERK/Akt phosphorylation.

Dietary vanadium overexposure in ducks was associated with lower NADH/FSP1/CoQ10-axis measures and increased hepatic lipid peroxidation and Fe2+ accumulation.

Vanadium-exposed duck livers showed wider ER–mitochondrial gaps and altered abundance/association of the IP3R–GRP75–VDAC1 contact complex.

In the 16-person six-week type-2-diabetes trial, clamp glucose metabolism did not improve at 75 mg/day VOSO4; improvement occurred in three of five at 150 mg/day and four of eight at 300 mg/day.

Basal hepatic glucose production and its insulin suppression were unchanged at all three doses in the 16-person trial.

After vanadyl treatment, muscle showed trends toward increased basal insulin-receptor, IRS1 and Shc tyrosine phosphorylation and IRS1-associated PI3K activity without additional insulin-stimulated increases.

Vanadyl did not change basal or insulin-stimulated muscle glycogen-synthase activity in the six-week study.

The 150- and 300-mg/day sulfate regimens caused some gastrointestinal intolerance during the six-week trial.

Total serum vanadium was not significantly correlated with insulin sensitivity in the pharmacokinetic analysis of the 16-person trial.

The fitted serum elimination half-times averaged about 4.7 and 4.6 days in the 50- and 100-mg elemental-V/day groups.

Daily urinary recovery was roughly 1% or less of administered elemental V in the trial, used by the authors to estimate low oral absorption.

In eight patients given 50 mg vanadyl sulfate twice daily for four weeks, fasting glucose and hepatic glucose output during insulin infusion decreased, without significant whole-body glucose-uptake improvement.

Seven healthy active adults showed no improvement in fasting glucose, fasting insulin or OGTT-derived insulin-sensitivity index after one or seven days of vanadyl sulfate.

The transferrin-cycle model supported by the binding experiments releases iron in acidified endosomes while apotransferrin remains receptor-bound.

Steap3 colocalized with transferrin-cycle endosomes and promoted iron reduction and transferrin-dependent iron uptake.

FSP1 used NAD(P)H to regenerate the reduced CoQ pool that traps lipid peroxyl radicals.

Lipoic acid reduced phosphatase activity and PTP1B thiol reactivity in 3T3-L1 cells.

Obese rats receiving chromium picolinate had lower muscle PTP1B abundance and lower activity after correction for protein content.

CGA showed noncompetitive PTP1B inhibition in the combined kinetic and NMR investigation.

Hippocampal neuronal-specific PTP1B deletion prevented olanzapine-induced synaptic and cognitive deficits in mice.

Availability and dependencies

The sources

Recorded disagreements

Open questions in this collection